English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/215658
Share/Impact:
Statistics
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE
Exportar a otros formatos:

Title

Linking the landscape of MYH9-related diseases to the molecular mechanisms that control non-muscle myosin II-A function in cells

AuthorsAsensio-Juárez, Gloria; Llorente-González, Clara; Vicente-Manzanares, Miguel
KeywordsMYH9
Myosin
Actin
Macrothrombocytopenia
Filament
Motor activity
Polymerization
Issue Date12-Jun-2020
PublisherMultidisciplinary Digital Publishing Institute
CitationCells 9(6): 1458 (2020)
AbstractThe MYH9 gene encodes the heavy chain (MHCII) of non-muscle myosin II A (NMII-A). This is an actin-binding molecular motor essential for development that participates in many crucial cellular processes such as adhesion, cell migration, cytokinesis and polarization, maintenance of cell shape and signal transduction. Several types of mutations in the MYH9 gene cause an array of autosomal dominant disorders, globally known as MYH9-related diseases (MYH9-RD). These include May-Hegglin anomaly (MHA), Epstein syndrome (EPS), Fechtner syndrome (FTS) and Sebastian platelet syndrome (SPS). Although caused by different MYH9 mutations, all patients present macrothrombocytopenia, but may later display other pathologies, including loss of hearing, renal failure and presenile cataracts. The correlation between the molecular and cellular effects of the different mutations and clinical presentation are beginning to be established. In this review, we correlate the defects that MYH9 mutations cause at a molecular and cellular level (for example, deficient filament formation, altered ATPase activity or actin-binding) with the clinical presentation of the syndromes in human patients. We address why these syndromes are tissue restricted, and the existence of possible compensatory mechanisms, including residual activity of mutant NMII-A and/or the formation of heteropolymers or co-polymers with other NMII isoforms.
DescriptionThis article belongs to the Special Issue Actin-Myosin Cytoskeleton Regulation and Function.
Publisher version (URL)https://doi.org/10.3390/cells9061458
URIhttp://hdl.handle.net/10261/215658
DOIhttp://dx.doi.org/10.3390/cells9061458
ISSN2073-4409
E-ISSN2073-4409
Appears in Collections:(IBMCC) Artículos
Files in This Item:
File Description SizeFormat 
Linking_Asensio_Juarez_Art2020.pdf2,61 MBAdobe PDFThumbnail
View/Open
Show full item record
Review this work
 


WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.